DOI: https://doi.org/10.61435/jbes.2024.19940

Kinetic features and characterization of liver glutathione transferase in rats exposed to glyphosate

1Department of Biochemistry, College of Biosciences, Federal University of Agriculture, Abeokuta, Nigeria

2Department of Animal Nutrition, College of Animal Science and Livestock Production, Federal University of Agriculture, Abeokuta, Nigeria

3Department of Biochemistry, College of Health Sciences, Osun State University, Osogbo, Nigeria

4 Department of Biochemistry, Faculty of Natural and Applied Sciences, Lead City University, Ibadan, Nigeria

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Received: 22 Jul 2024; Revised: 8 Oct 2024; Accepted: 3 Dec 2024; Available online: 3 Feb 2025; Published: 1 Apr 2025.
Editor(s): H. Hadiyanto
Open Access Copyright (c) 2025 The Author(s). Published by Centre of Biomass and Renewable Energy (CBIORE)
Creative Commons License This work is licensed under a Creative Commons Attribution 4.0 International License.

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Abstract

Glutathione-S-transferases (GSTs) are phase-II metabolizing enzymes which detoxify various compounds through their conjugation reaction. This study characterized and investigated the kinetic properties of liver glutathione-S-transferase in rats exposed to glyphosate. Rats of average weight 200 g were randomly divided into groups (n=4); A, B, C and D. Group A served as control and received distilled water alone while groups B, C and D were exposed to 200, 300 and 400 mg/kg body weight of glyphosate respectively. Three GST model substrates [1, 2-dichloro-4-nitrobenzene (DCNB), paranitrobenzylchloride (pNBCl), and 1-chloro-2, 4-dinitrobenzene (CDNB)] were used to determine the substrate utilization pattern of the GST isozymes in the liver crude homogenate. The liver homogenate was purified by combination of 80 % ammonium sulfate precipitation, gel filtration chromatography on Sephacryl S-200 column and ion exchange chromatography on CM-Sepharose column. Spectrophotometric methods were used to determine the activity of the GSTs and protein concentration. GST isozymes in the liver homogenate were unable to conjugate pNBCl to GSH, DCNB showed slight conjugation while CDNB shows a 2-fold conjugation. The optimum temperature for the induced isozymes of GST A and GST B were 400C and 500C respectively while the optimum pH were 8.0 and 8.5 respectively. In this study, pNBCl proved unsuitable due to its inability to conjugate GSH. Future study may provide additional information about the class of GST isozyme induced.

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Keywords: Glutathione transferase (GST); Glyphosate; Metal ions; Thiol reagents

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